Full text data of NUBP1
NUBP1
(NBP, NBP1)
[Confidence: low (only semi-automatic identification from reviews)]
Cytosolic Fe-S cluster assembly factor NUBP1 (Nucleotide-binding protein 1; NBP 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cytosolic Fe-S cluster assembly factor NUBP1 (Nucleotide-binding protein 1; NBP 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P53384
ID NUBP1_HUMAN Reviewed; 320 AA.
AC P53384; Q32M30; Q498A9; Q53FS7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-SEP-2009, sequence version 2.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP1;
DE AltName: Full=Nucleotide-binding protein 1;
DE Short=NBP 1;
GN Name=NUBP1; Synonyms=NBP, NBP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7926816; DOI=10.1016/0378-1119(94)90082-5;
RA Shahrestanifar M., Saha D.P., Scala L.A., Basu A., Howells R.D.;
RT "Cloning of a human cDNA encoding a putative nucleotide-binding
RT protein related to Escherichia coli MinD.";
RL Gene 147:281-285(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ALA-39.
RC TISSUE=Spleen;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-39.
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, INTERACTION WITH NUBP2, SUBCELLULAR LOCATION, AND EPR
RP SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
RX PubMed=18573874; DOI=10.1128/MCB.00545-08;
RA Stehling O., Netz D.J.A., Niggemeyer B., Roesser R., Eisenstein R.S.,
RA Puccio H., Pierik A.J., Lill R.;
RT "Human Nbp35 is essential for both cytosolic iron-sulfur protein
RT assembly and iron homeostasis.";
RL Mol. Cell. Biol. 28:5517-5528(2008).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Implicated in the regulation of centrosome duplication
CC (By similarity). Component of the cytosolic iron-sulfur (Fe/S)
CC protein assembly (CIA) machinery. Required for maturation of
CC extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer
CC forms a Fe-S scaffold complex, mediating the de novo assembly of
CC an Fe-S cluster and its transfer to target apoproteins.
CC -!- COFACTOR: Binds 4 4Fe-4S clusters per heterotetramer. Contains two
CC stable clusters in the N-termini of NUBP1 and two labile, bridging
CC clusters between subunits of the NUBP1-NUBP2 heterotetramer (By
CC similarity).
CC -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains. Interacts
CC with KIFC1 (By similarity). Interacts with NUBP2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P53384-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53384-2; Sequence=VSP_029043;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP1/NBP35 subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U01833; AAA61932.1; -; mRNA.
DR EMBL; AK223204; BAD96924.1; -; mRNA.
DR EMBL; BC100290; AAI00291.1; -; mRNA.
DR EMBL; BC109322; AAI09323.1; -; mRNA.
DR EMBL; BC109323; AAI09324.1; -; mRNA.
DR PIR; JC4010; JC4010.
DR RefSeq; NP_001265435.1; NM_001278506.1.
DR RefSeq; NP_002475.2; NM_002484.3.
DR UniGene; Hs.81469; -.
DR ProteinModelPortal; P53384; -.
DR SMR; P53384; 44-309.
DR IntAct; P53384; 1.
DR MINT; MINT-3019860; -.
DR STRING; 9606.ENSP00000283027; -.
DR PhosphoSite; P53384; -.
DR DMDM; 257050984; -.
DR PaxDb; P53384; -.
DR PRIDE; P53384; -.
DR Ensembl; ENST00000283027; ENSP00000283027; ENSG00000103274.
DR Ensembl; ENST00000433392; ENSP00000409654; ENSG00000103274.
DR GeneID; 4682; -.
DR KEGG; hsa:4682; -.
DR UCSC; uc002daa.1; human.
DR CTD; 4682; -.
DR GeneCards; GC16P010837; -.
DR H-InvDB; HIX0038641; -.
DR HGNC; HGNC:8041; NUBP1.
DR HPA; HPA041656; -.
DR HPA; HPA041799; -.
DR MIM; 600280; gene.
DR neXtProt; NX_P53384; -.
DR PharmGKB; PA31823; -.
DR eggNOG; COG0489; -.
DR HOGENOM; HOG000079916; -.
DR HOVERGEN; HBG051027; -.
DR InParanoid; P53384; -.
DR OMA; QDLEVPL; -.
DR PhylomeDB; P53384; -.
DR Reactome; REACT_111217; Metabolism.
DR GenomeRNAi; 4682; -.
DR NextBio; 18050; -.
DR PRO; PR:P53384; -.
DR ArrayExpress; P53384; -.
DR Bgee; P53384; -.
DR CleanEx; HS_NUBP1; -.
DR Genevestigator; P53384; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; TAS:ProtInc.
DR GO; GO:0016049; P:cell growth; IMP:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR HAMAP; MF_03038; NUBP1; 1; -.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR025723; Anion-transp_ATPase-like_dom.
DR InterPro; IPR019591; ATPase-like_ParA/MinD.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR028601; NUBP1/Nbp35.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02374; ArsA_ATPase; 1.
DR Pfam; PF10609; ParA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Polymorphism; Reference proteome.
FT CHAIN 1 320 Cytosolic Fe-S cluster assembly factor
FT NUBP1.
FT /FTId=PRO_0000184943.
FT NP_BIND 62 69 ATP (Potential).
FT METAL 8 8 Iron-sulfur 1 (4Fe-4S) (By similarity).
FT METAL 22 22 Iron-sulfur 1 (4Fe-4S) (By similarity).
FT METAL 25 25 Iron-sulfur 1 (4Fe-4S) (By similarity).
FT METAL 31 31 Iron-sulfur 1 (4Fe-4S) (By similarity).
FT METAL 235 235 Iron-sulfur 2 (4Fe-4S); shared with
FT dimeric partner (By similarity).
FT METAL 238 238 Iron-sulfur 2 (4Fe-4S); shared with
FT dimeric partner (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 110 120 Missing (in isoform 2).
FT /FTId=VSP_029043.
FT VARIANT 39 39 P -> A (in dbSNP:rs2233531).
FT /FTId=VAR_020359.
FT CONFLICT 204 204 V -> L (in Ref. 1; AAA61932).
FT CONFLICT 232 232 G -> P (in Ref. 1; AAA61932).
SQ SEQUENCE 320 AA; 34534 MW; 346E1C694224E437 CRC64;
MEEVPHDCPG ADSAQAGRGA SCQGCPNQRL CASGAGATPD TAIEEIKEKM KTVKHKILVL
SGKGGVGKST FSAHLAHGLA EDENTQIALL DIDICGPSIP KIMGLEGEQV HQSGSGWSPV
YVEDNLGVMS VGFLLSSPDD AVIWRGPKKN GMIKQFLRDV DWGEVDYLIV DTPPGTSDEH
LSVVRYLATA HIDGAVIITT PQEVSLQDVR KEINFCRKVK LPIIGVVENM SGFICPKCKK
ESQIFPPTTG GAELMCQDLE VPLLGRVPLD PLIGKNCDKG QSFFIDAPDS PATLAYRSII
QRIQEFCNLH QSKEENLISS
//
ID NUBP1_HUMAN Reviewed; 320 AA.
AC P53384; Q32M30; Q498A9; Q53FS7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-SEP-2009, sequence version 2.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP1;
DE AltName: Full=Nucleotide-binding protein 1;
DE Short=NBP 1;
GN Name=NUBP1; Synonyms=NBP, NBP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7926816; DOI=10.1016/0378-1119(94)90082-5;
RA Shahrestanifar M., Saha D.P., Scala L.A., Basu A., Howells R.D.;
RT "Cloning of a human cDNA encoding a putative nucleotide-binding
RT protein related to Escherichia coli MinD.";
RL Gene 147:281-285(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ALA-39.
RC TISSUE=Spleen;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-39.
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, INTERACTION WITH NUBP2, SUBCELLULAR LOCATION, AND EPR
RP SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
RX PubMed=18573874; DOI=10.1128/MCB.00545-08;
RA Stehling O., Netz D.J.A., Niggemeyer B., Roesser R., Eisenstein R.S.,
RA Puccio H., Pierik A.J., Lill R.;
RT "Human Nbp35 is essential for both cytosolic iron-sulfur protein
RT assembly and iron homeostasis.";
RL Mol. Cell. Biol. 28:5517-5528(2008).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Implicated in the regulation of centrosome duplication
CC (By similarity). Component of the cytosolic iron-sulfur (Fe/S)
CC protein assembly (CIA) machinery. Required for maturation of
CC extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer
CC forms a Fe-S scaffold complex, mediating the de novo assembly of
CC an Fe-S cluster and its transfer to target apoproteins.
CC -!- COFACTOR: Binds 4 4Fe-4S clusters per heterotetramer. Contains two
CC stable clusters in the N-termini of NUBP1 and two labile, bridging
CC clusters between subunits of the NUBP1-NUBP2 heterotetramer (By
CC similarity).
CC -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains. Interacts
CC with KIFC1 (By similarity). Interacts with NUBP2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P53384-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53384-2; Sequence=VSP_029043;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP1/NBP35 subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U01833; AAA61932.1; -; mRNA.
DR EMBL; AK223204; BAD96924.1; -; mRNA.
DR EMBL; BC100290; AAI00291.1; -; mRNA.
DR EMBL; BC109322; AAI09323.1; -; mRNA.
DR EMBL; BC109323; AAI09324.1; -; mRNA.
DR PIR; JC4010; JC4010.
DR RefSeq; NP_001265435.1; NM_001278506.1.
DR RefSeq; NP_002475.2; NM_002484.3.
DR UniGene; Hs.81469; -.
DR ProteinModelPortal; P53384; -.
DR SMR; P53384; 44-309.
DR IntAct; P53384; 1.
DR MINT; MINT-3019860; -.
DR STRING; 9606.ENSP00000283027; -.
DR PhosphoSite; P53384; -.
DR DMDM; 257050984; -.
DR PaxDb; P53384; -.
DR PRIDE; P53384; -.
DR Ensembl; ENST00000283027; ENSP00000283027; ENSG00000103274.
DR Ensembl; ENST00000433392; ENSP00000409654; ENSG00000103274.
DR GeneID; 4682; -.
DR KEGG; hsa:4682; -.
DR UCSC; uc002daa.1; human.
DR CTD; 4682; -.
DR GeneCards; GC16P010837; -.
DR H-InvDB; HIX0038641; -.
DR HGNC; HGNC:8041; NUBP1.
DR HPA; HPA041656; -.
DR HPA; HPA041799; -.
DR MIM; 600280; gene.
DR neXtProt; NX_P53384; -.
DR PharmGKB; PA31823; -.
DR eggNOG; COG0489; -.
DR HOGENOM; HOG000079916; -.
DR HOVERGEN; HBG051027; -.
DR InParanoid; P53384; -.
DR OMA; QDLEVPL; -.
DR PhylomeDB; P53384; -.
DR Reactome; REACT_111217; Metabolism.
DR GenomeRNAi; 4682; -.
DR NextBio; 18050; -.
DR PRO; PR:P53384; -.
DR ArrayExpress; P53384; -.
DR Bgee; P53384; -.
DR CleanEx; HS_NUBP1; -.
DR Genevestigator; P53384; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; TAS:ProtInc.
DR GO; GO:0016049; P:cell growth; IMP:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR HAMAP; MF_03038; NUBP1; 1; -.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR025723; Anion-transp_ATPase-like_dom.
DR InterPro; IPR019591; ATPase-like_ParA/MinD.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR028601; NUBP1/Nbp35.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02374; ArsA_ATPase; 1.
DR Pfam; PF10609; ParA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Polymorphism; Reference proteome.
FT CHAIN 1 320 Cytosolic Fe-S cluster assembly factor
FT NUBP1.
FT /FTId=PRO_0000184943.
FT NP_BIND 62 69 ATP (Potential).
FT METAL 8 8 Iron-sulfur 1 (4Fe-4S) (By similarity).
FT METAL 22 22 Iron-sulfur 1 (4Fe-4S) (By similarity).
FT METAL 25 25 Iron-sulfur 1 (4Fe-4S) (By similarity).
FT METAL 31 31 Iron-sulfur 1 (4Fe-4S) (By similarity).
FT METAL 235 235 Iron-sulfur 2 (4Fe-4S); shared with
FT dimeric partner (By similarity).
FT METAL 238 238 Iron-sulfur 2 (4Fe-4S); shared with
FT dimeric partner (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 110 120 Missing (in isoform 2).
FT /FTId=VSP_029043.
FT VARIANT 39 39 P -> A (in dbSNP:rs2233531).
FT /FTId=VAR_020359.
FT CONFLICT 204 204 V -> L (in Ref. 1; AAA61932).
FT CONFLICT 232 232 G -> P (in Ref. 1; AAA61932).
SQ SEQUENCE 320 AA; 34534 MW; 346E1C694224E437 CRC64;
MEEVPHDCPG ADSAQAGRGA SCQGCPNQRL CASGAGATPD TAIEEIKEKM KTVKHKILVL
SGKGGVGKST FSAHLAHGLA EDENTQIALL DIDICGPSIP KIMGLEGEQV HQSGSGWSPV
YVEDNLGVMS VGFLLSSPDD AVIWRGPKKN GMIKQFLRDV DWGEVDYLIV DTPPGTSDEH
LSVVRYLATA HIDGAVIITT PQEVSLQDVR KEINFCRKVK LPIIGVVENM SGFICPKCKK
ESQIFPPTTG GAELMCQDLE VPLLGRVPLD PLIGKNCDKG QSFFIDAPDS PATLAYRSII
QRIQEFCNLH QSKEENLISS
//
MIM
600280
*RECORD*
*FIELD* NO
600280
*FIELD* TI
*600280 NUCLEOTIDE-BINDING PROTEIN 1; NUBP1
;;NBP;;
NBP35
*FIELD* TX
DESCRIPTION
read moreNUBP1 is a member of the NUBP/MRP subfamily of ATP-binding proteins
(Nakashima et al., 1999).
CLONING
By screening a human neuroblastoma library, Shahrestanifar et al. (1994)
cloned NUBP1, which they called NBP. The deduced 320-amino acid protein
has a molecular mass of 34.5 kD. NBP displays sequence similarity with
the product of the MinD gene from Escherichia coli. MinD is involved in
the proper placement of the division septum and has ATPase activity.
Both NBP and MinD contain consensus nucleotide-binding domains. The NBP
mRNA is approximately 1,500 nucleotides long and was expressed in
several human cell lines and in all rat tissues examined, with the
highest levels in lung and testis. Shahrestanifar et al. (1994)
indicated that the yeast homolog of the NBP gene had been isolated and
found to exhibit 40% identity with human NBP. Furthermore, mutation of
the gene was found to be lethal in yeast, indicating that NBP plays a
vital role in cell function.
Nakashima et al. (1999) showed that NUBP1 contains a conserved ATP/GTP
binding motif A (P-loop), an ATP/GTP binding motif A-prime, and NUBP/MRP
alpha and beta motifs. NUBP1 has an additional N-terminal sequence with
4 cysteine residues that is not present in NUBP2 (610779).
Stehling et al. (2008) noted that the N and C termini of human NBP35
have several conserved cysteines that may form iron-binding sites. Using
ultraviolet and visible spectroscopy and low-temperature electron
paramagnetic resonance, they showed that NBP35 likely coordinated a
4Fe-4S cluster. Both fluorescence-tagged and endogenous HeLa cell NBP35
localized to the cytosol, which was verified by cell fractionation.
GENE FUNCTION
Stehling et al. (2008) found that depletion of NBP35 in HeLa cells via
RNA interference impaired maturation of the cytosolic Fe-S proteins GPAT
(PPAT; 172450) and IRP1 (ACO1; 100880). IRP1 is a bifunctional protein;
in the presence of a 4Fe-4S cluster, it functions as a cytosolic
aconitase, and in the absence of a 4Fe-4S cluster, it regulates cellular
iron homeostasis by binding iron regulatory elements (IREs) in target
mRNAs, influencing mRNA translation. Depletion of NBP35 in HeLa cells
resulted in a time-dependent decrease in IRP1 cytosolic aconitase
activity and a concomitant increase in IRP1 binding to IREs. Binding of
IRP1 to a 5-prime IRE in ferritin heavy chain (FTH1; 134770) mRNA
inhibits translation and thereby reduces cytosolic iron storage
capacity, whereas binding of IRP1 to 3-prime IREs in transferrin
receptor (TFRC; 190010) mRNA stabilizes the mRNA, leading to increased
translation and increased uptake of transferrin (190000). Increased IRE
binding by IRP1 in NBP35-depleted cells led to decreased levels of
ferritin heavy chain, increased levels of transferrin receptor, and
increased transferrin uptake. NBP35 also interacted with coexpressed
CFD1 (NUBP2; 610779) in transfected HeLa cells, suggesting that the 2
proteins may function in a complex for regulation of cellular iron
homeostasis and cytosolic Fe-S protein assembly.
MAPPING
Hartz (2012) mapped the NUBP1 gene to chromosome 16p13.13 based on an
alignment of the NUBP1 sequence (GenBank GENBANK AK223204) with the
genomic sequence (GRCh37).
Nakashima et al. (1999) mapped the mouse Nubp1 gene to the t-complex
region of mouse chromosome 16, which shows homology of synteny with
human chromosome 16p13.1.
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 9/11/2012.
2. Nakashima, H.; Grahovac, M. J.; Mazzarella, R.; Fujiwara, H.; Kitchen,
J. R.; Threat, T. A.; Ko, M. S. H.: Two novel mouse genes--Nubp2,
mapped to the t-complex on chromosome 17, and Nubp1, mapped to the
chromosome 16--establish a new gene family of nucleotide-binding proteins
in eukaryotes. Genomics 60: 152-160, 1999.
3. Shahrestanifar, M.; Saha, D. P.; Scala, L. A.; Basu, A.; Howells,
R. D.: Cloning of a human cDNA encoding a putative nucleotide-binding
protein related to Escherichia coli MinD. Gene 147: 281-285, 1994.
4. Stehling, O.; Netz, D. J. A.; Niggemeyer, B.; Rosser, R.; Eisenstein,
R. S.; Puccio, H.; Pierik, A. J.; Lill, R.: Human Nbp35 is essential
for both cytosolic iron-sulfur protein assembly and iron homeostasis. Molec.
Cell. Biol. 28: 5517-5528, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 9/11/2012
Dorothy S. Reilly - updated: 2/21/2007
*FIELD* CD
Victor A. McKusick: 1/5/1995
*FIELD* ED
mgross: 09/17/2012
terry: 9/11/2012
wwang: 2/21/2007
carol: 6/4/1999
jamie: 5/7/1997
carol: 1/5/1995
*RECORD*
*FIELD* NO
600280
*FIELD* TI
*600280 NUCLEOTIDE-BINDING PROTEIN 1; NUBP1
;;NBP;;
NBP35
*FIELD* TX
DESCRIPTION
read moreNUBP1 is a member of the NUBP/MRP subfamily of ATP-binding proteins
(Nakashima et al., 1999).
CLONING
By screening a human neuroblastoma library, Shahrestanifar et al. (1994)
cloned NUBP1, which they called NBP. The deduced 320-amino acid protein
has a molecular mass of 34.5 kD. NBP displays sequence similarity with
the product of the MinD gene from Escherichia coli. MinD is involved in
the proper placement of the division septum and has ATPase activity.
Both NBP and MinD contain consensus nucleotide-binding domains. The NBP
mRNA is approximately 1,500 nucleotides long and was expressed in
several human cell lines and in all rat tissues examined, with the
highest levels in lung and testis. Shahrestanifar et al. (1994)
indicated that the yeast homolog of the NBP gene had been isolated and
found to exhibit 40% identity with human NBP. Furthermore, mutation of
the gene was found to be lethal in yeast, indicating that NBP plays a
vital role in cell function.
Nakashima et al. (1999) showed that NUBP1 contains a conserved ATP/GTP
binding motif A (P-loop), an ATP/GTP binding motif A-prime, and NUBP/MRP
alpha and beta motifs. NUBP1 has an additional N-terminal sequence with
4 cysteine residues that is not present in NUBP2 (610779).
Stehling et al. (2008) noted that the N and C termini of human NBP35
have several conserved cysteines that may form iron-binding sites. Using
ultraviolet and visible spectroscopy and low-temperature electron
paramagnetic resonance, they showed that NBP35 likely coordinated a
4Fe-4S cluster. Both fluorescence-tagged and endogenous HeLa cell NBP35
localized to the cytosol, which was verified by cell fractionation.
GENE FUNCTION
Stehling et al. (2008) found that depletion of NBP35 in HeLa cells via
RNA interference impaired maturation of the cytosolic Fe-S proteins GPAT
(PPAT; 172450) and IRP1 (ACO1; 100880). IRP1 is a bifunctional protein;
in the presence of a 4Fe-4S cluster, it functions as a cytosolic
aconitase, and in the absence of a 4Fe-4S cluster, it regulates cellular
iron homeostasis by binding iron regulatory elements (IREs) in target
mRNAs, influencing mRNA translation. Depletion of NBP35 in HeLa cells
resulted in a time-dependent decrease in IRP1 cytosolic aconitase
activity and a concomitant increase in IRP1 binding to IREs. Binding of
IRP1 to a 5-prime IRE in ferritin heavy chain (FTH1; 134770) mRNA
inhibits translation and thereby reduces cytosolic iron storage
capacity, whereas binding of IRP1 to 3-prime IREs in transferrin
receptor (TFRC; 190010) mRNA stabilizes the mRNA, leading to increased
translation and increased uptake of transferrin (190000). Increased IRE
binding by IRP1 in NBP35-depleted cells led to decreased levels of
ferritin heavy chain, increased levels of transferrin receptor, and
increased transferrin uptake. NBP35 also interacted with coexpressed
CFD1 (NUBP2; 610779) in transfected HeLa cells, suggesting that the 2
proteins may function in a complex for regulation of cellular iron
homeostasis and cytosolic Fe-S protein assembly.
MAPPING
Hartz (2012) mapped the NUBP1 gene to chromosome 16p13.13 based on an
alignment of the NUBP1 sequence (GenBank GENBANK AK223204) with the
genomic sequence (GRCh37).
Nakashima et al. (1999) mapped the mouse Nubp1 gene to the t-complex
region of mouse chromosome 16, which shows homology of synteny with
human chromosome 16p13.1.
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 9/11/2012.
2. Nakashima, H.; Grahovac, M. J.; Mazzarella, R.; Fujiwara, H.; Kitchen,
J. R.; Threat, T. A.; Ko, M. S. H.: Two novel mouse genes--Nubp2,
mapped to the t-complex on chromosome 17, and Nubp1, mapped to the
chromosome 16--establish a new gene family of nucleotide-binding proteins
in eukaryotes. Genomics 60: 152-160, 1999.
3. Shahrestanifar, M.; Saha, D. P.; Scala, L. A.; Basu, A.; Howells,
R. D.: Cloning of a human cDNA encoding a putative nucleotide-binding
protein related to Escherichia coli MinD. Gene 147: 281-285, 1994.
4. Stehling, O.; Netz, D. J. A.; Niggemeyer, B.; Rosser, R.; Eisenstein,
R. S.; Puccio, H.; Pierik, A. J.; Lill, R.: Human Nbp35 is essential
for both cytosolic iron-sulfur protein assembly and iron homeostasis. Molec.
Cell. Biol. 28: 5517-5528, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 9/11/2012
Dorothy S. Reilly - updated: 2/21/2007
*FIELD* CD
Victor A. McKusick: 1/5/1995
*FIELD* ED
mgross: 09/17/2012
terry: 9/11/2012
wwang: 2/21/2007
carol: 6/4/1999
jamie: 5/7/1997
carol: 1/5/1995